ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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T-complex protein 1 subunit gamma

Intermolecular
Cysteine 213 and cysteine 213
Intramolecular
Cysteine 366 and cysteine 372
Cysteine 327 and cysteine 366
Cysteine 327 and cysteine 372
Cysteine 213 and cysteine 372
Cysteine 173 and cysteine 398 L
Cysteine 372 and cysteine 398 L
A redox-regulated disulphide may form between two units of T-complex protein 1 subunit gamma at cysteines 213 and 213.

Details

Redox score ?
74
PDB code
1gml
Structure name
crystal structure of the mouse cct gamma apical domain (triclinic)
Structure deposition date
2001-09-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
34
Minimum pKa ?
9
% buried
0
Peptide A name
T-complex protein 1 subunit gamma
Peptide B name
T-complex protein 1 subunit gamma
Peptide A accession
P80318
Peptide B accession
P80318
Peptide A residue number
213
Peptide B residue number
213

Ligandability

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within T-complex protein 1 subunit gamma between cysteines 366 and 372.

Details

Redox score ?
86
PDB code
1gn1
Structure name
crystal structure of the mouse cct gamma apical domain (monoclinic)
Structure deposition date
2001-10-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P80318
Residue number A
366
Residue number B
372
Peptide name
T-complex protein 1 subunit gamma

Ligandability

Cysteine 366 of T-complex protein 1 subunit gamma

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 372 of T-complex protein 1 subunit gamma

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within T-complex protein 1 subunit gamma between cysteines 327 and 366. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
7nvn
Structure name
human tric complex in closed state with nanobody and tubulin bound
Structure deposition date
2021-03-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
87
Peptide accession
P49368
Residue number A
327
Residue number B
366
Peptide name
T-complex protein 1 subunit gamma

Ligandability

Cysteine 327 of T-complex protein 1 subunit gamma

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 366 of T-complex protein 1 subunit gamma

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within T-complex protein 1 subunit gamma between cysteines 327 and 372. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1gn1
Structure name
crystal structure of the mouse cct gamma apical domain (monoclinic)
Structure deposition date
2001-10-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
nan
Peptide accession
P80318
Residue number A
327
Residue number B
372
Peptide name
T-complex protein 1 subunit gamma

Ligandability

Cysteine 327 of T-complex protein 1 subunit gamma

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 372 of T-complex protein 1 subunit gamma

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within T-complex protein 1 subunit gamma between cysteines 213 and 372. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7lup
Structure name
human tric/cct complex with reovirus outer capsid protein sigma-3
Structure deposition date
2021-02-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
10
% buried
61
Peptide accession
P49368
Residue number A
213
Residue number B
372
Peptide name
T-complex protein 1 subunit gamma

Ligandability

Cysteine 213 of T-complex protein 1 subunit gamma

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 372 of T-complex protein 1 subunit gamma

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within T-complex protein 1 subunit gamma between cysteines 173 and 398 (1173 and 1398 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4b2t
Structure name
the crystal structures of the eukaryotic chaperonin cct reveal its functional partitioning
Structure deposition date
2012-07-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
11
% buried
66
Peptide accession
Q3T0K2
Residue number A
173
Residue number B
398
Peptide name
T-complex protein 1 subunit gamma

Ligandability

Cysteine 173 of T-complex protein 1 subunit gamma

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 398 of T-complex protein 1 subunit gamma

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within T-complex protein 1 subunit gamma between cysteines 372 and 398. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
22
PDB code
6nrd
Structure name
htric-hpfd class4
Structure deposition date
2019-01-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
101
Minimum pKa ?
12
% buried
100
Peptide accession
P49368
Residue number A
372
Residue number B
398
Peptide name
T-complex protein 1 subunit gamma

Ligandability

Cysteine 372 of T-complex protein 1 subunit gamma

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 398 of T-complex protein 1 subunit gamma

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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